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Atomistry » Magnesium » PDB 3fcw-3fpk » 3feg » |
Magnesium in PDB 3feg: Crystal Structure of Human Choline Kinase Beta in Complex with Phosphorylated Hemicholinium-3 and Adenosine NucleotideEnzymatic activity of Crystal Structure of Human Choline Kinase Beta in Complex with Phosphorylated Hemicholinium-3 and Adenosine Nucleotide
All present enzymatic activity of Crystal Structure of Human Choline Kinase Beta in Complex with Phosphorylated Hemicholinium-3 and Adenosine Nucleotide:
2.7.1.32; 2.7.1.82; Protein crystallography data
The structure of Crystal Structure of Human Choline Kinase Beta in Complex with Phosphorylated Hemicholinium-3 and Adenosine Nucleotide, PDB code: 3feg
was solved by
B.S.Hong,
W.Tempel,
W.M.Rabeh,
F.Mackenzie,
C.H.Arrowsmith,
A.M.Edwards,
C.Bountra,
J.Weigelt,
A.Bochkarev,
H.W.Park,
Structural Genomicsconsortium (Sgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Human Choline Kinase Beta in Complex with Phosphorylated Hemicholinium-3 and Adenosine Nucleotide
(pdb code 3feg). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Human Choline Kinase Beta in Complex with Phosphorylated Hemicholinium-3 and Adenosine Nucleotide, PDB code: 3feg: Magnesium binding site 1 out of 1 in 3fegGo back to Magnesium Binding Sites List in 3feg
Magnesium binding site 1 out
of 1 in the Crystal Structure of Human Choline Kinase Beta in Complex with Phosphorylated Hemicholinium-3 and Adenosine Nucleotide
Mono view Stereo pair view
Reference:
B.S.Hong,
A.Allali-Hassani,
W.Tempel,
P.J.Finerty,
F.Mackenzie,
S.Dimov,
M.Vedadi,
H.W.Park.
Crystal Structures of Human Choline Kinase Isoforms in Complex with Hemicholinium-3: Single Amino Acid Near the Active Site Influences Inhibitor Sensitivity. J.Biol.Chem. V. 285 16330 2010.
Page generated: Wed Aug 14 13:45:34 2024
ISSN: ISSN 0021-9258 PubMed: 20299452 DOI: 10.1074/JBC.M109.039024 |
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